Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4

被引:76
作者
Zendo, Takeshi
Koga, Shoko
Shigeri, Yasushi
Nakayama, Jiro
Sonomoto, Kenji
机构
[1] Kyushu Univ, Lab Microbial Technol, Div Microbial Sci & Technol,Higashi Ku, Dept Biosci & Biotechnol,Fac Agr,Grad Sch, Fukuoka 8128581, Japan
[2] Kyushu Univ, Dept Funct Metab Design, BioArchitecture Ctr, Higashi Ku, Fukuoka 8128581, Japan
[3] Natl Inst Adv Ind Sci & Technol, Res Inst Cell Engn, Ikeda, Osaka 5638577, Japan
关键词
D O I
10.1128/AEM.72.5.3383-3389.2006
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A bacteriocin-producing strain, Lactococcus lactis QU 4, was isolated from corn. The bacteriocin, termed lactococcin Q, showed antibacterial activity only against L. lactis strains among a wide range of gram-positive indicator strains tested. Lactococcin Q was purified by acetone precipitation, cation exchange chromatography, and reverse-phase chromatography. Lactococcin Q consisted of two peptides, alpha and beta, whose molecular masses were determined to be 4,260.43 Da and 4,018.36 Da, respectively. Amino acid and DNA sequencing analyses revealed that lactococcin Q was a novel two-peptide bacteriocin, homologous to lactococcin G. Comparative study using chemically synthesized lactococcin Q (Q alpha plus Q beta) and lactococcin G (G alpha plus G beta) clarified that hybrid combinations (Q alpha plus G beta and G alpha plus Q beta) as well as original combinations showed antibacterial activity, although each single peptide showed no significant activity. These four pairs of lactococcin peptides acted synergistically at a 1:1 molar ratio and exhibited identical antibacterial spectra but differed in MIC. The MIC of Q alpha plus G beta was 32 times higher than that of Q alpha plus Q beta, suggesting that the difference in beta peptides was important for the intensity of antibacterial activity.
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页码:3383 / 3389
页数:7
相关论文
共 33 条
  • [1] Ausubel FM, 1995, CURRENT PROTOCOLS MO
  • [2] Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071
    Balla, E
    Dicks, LMT
    Du Toit, M
    van der Merwe, MJ
    Holzapfel, WH
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (04) : 1298 - 1304
  • [3] Bacteriocins: safe, natural antimicrobials for food preservation
    Cleveland, J
    Montville, TJ
    Nes, IF
    Chikindas, ML
    [J]. INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY, 2001, 71 (01) : 1 - 20
  • [4] Isolation, purification, and amino acid sequence of lactobin A, one of the two bacteriocins produced by Lactobacillus amylovorus LMG p-13139
    Contreras, BGL
    DeVuyst, L
    Devreese, B
    Busanyova, K
    Raymaeckers, J
    Bosman, F
    Sablon, E
    Vandamme, EJ
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1997, 63 (01) : 13 - 20
  • [5] Biochemical and genetic evidence for production of enterocins A and B by Enterococcus faecium WHE 81
    Ennahar, S
    Asou, Y
    Zendo, T
    Sonomoto, K
    Ishizaki, A
    [J]. INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY, 2001, 70 (03) : 291 - 301
  • [6] Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp salivarius UCC118
    Flynn, S
    van Sinderen, D
    Thornton, GM
    Holo, H
    Nes, IF
    Collins, JK
    [J]. MICROBIOLOGY-SGM, 2002, 148 : 973 - 984
  • [7] Biochemical and genetic characterization of the two-peptide bacteriocin enterocin 1071 produced by Enterococcus faecalis FAIR-E 309
    Franz, CMAP
    Grube, A
    Herrmann, A
    Abriouel, H
    Stärke, J
    Lombardi, A
    Tauscher, B
    Holzapfel, WH
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2002, 68 (05) : 2550 - 2554
  • [8] Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins
    Gajic, O
    Buist, G
    Kojic, M
    Topisirovic, L
    Kuipers, OP
    Kok, J
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (36) : 34291 - 34298
  • [9] Two-peptide bacteriocins produced by lactic acid bacteria
    Garneau, S
    Martin, NI
    Vederas, JC
    [J]. BIOCHIMIE, 2002, 84 (5-6) : 577 - 592
  • [10] Amphiphilic α-helices are important structural motifs in the α and β peptides that constitute the bacteriocin lactococcin G -: Enhancement of helix formation upon α-β interaction
    Hauge, HH
    Nissen-Meyer, J
    Nes, IF
    Eijsink, VGH
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 251 (03): : 565 - 572